J
Jei-Fu Shaw
Researcher at I-Shou University
Publications - 130
Citations - 5157
Jei-Fu Shaw is an academic researcher from I-Shou University. The author has contributed to research in topics: Lipase & Candida rugosa. The author has an hindex of 38, co-authored 127 publications receiving 4777 citations. Previous affiliations of Jei-Fu Shaw include National Cheng Kung University & National Chung Hsing University.
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GDSL family of serine esterases/lipases.
TL;DR: Much still needs to be done to gain better understanding of in vivo biological function, 3-D structure, how this group of enzymes evolved to utilize many different substrates, and the mechanism of reactions, as well as understanding the conformational changes.
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Enzymatic Approach to Biodiesel Production
TL;DR: The use of recombinant DNA technology to produce large quantities of lipases, and the use of immobilized lipases and immobilized whole cells, may lower the overall cost, while presenting less downstream processing problems, to biodiesel production.
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Multifunctionality and diversity of GDSL esterase/lipase gene family in rice ( Oryza sativa L. japonica ) genome: new insights from bioinformatics analysis
TL;DR: The genomic, phylogenetic, microarray expression, protein motif distribution, and protein structure analyses were able to create supported basis for the functional prediction of many members in the rice GDSL esterase/lipase family.
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Lipolytic activities of a lipase immobilized on six selected supporting materials
TL;DR: Lipase immobilized on PVC exhibited higher thermal stability than that on agarose and the specific activity of the immobilized lipase was affected by the pore size but not by the chain length of the hydrocarbon attached to the support.
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Crystal Structure of Escherichia coli Thioesterase I/Protease I/Lysophospholipase L1: Consensus Sequence Blocks Constitute the Catalytic Center of SGNH-hydrolases through a Conserved Hydrogen Bond Network
TL;DR: It is proposed that the existence of the highly polarized tri-residue-constituted oxyanion hole compensates for the lack of a (His)C(epsilon1)-H...O=C hydrogen bond, which suggests that members of the SGNH-hydrolase family may employ a unique catalytic mechanism.